Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Drosophila mutant methuselah (mth) was identified from a screen for single gene mutations that extended average lifespan. Mth mutants have a 35% increase in average lifespan and increased resistance to several forms of stress, including heat, starvation, and oxidative damage. The protein affected by this mutation is related to G protein-coupled receptors of the secretin receptor family. Mth, like secretin receptor family members, has a large N-terminal ectodomain, which may constitute the ligand binding site. Here we report the 2.3-A resolution crystal structure of the Mth extracellular region, revealing a folding topology in which three primarily beta-structure-containing domains meet to form a shallow interdomain groove containing a solvent-exposed tryptophan that may represent a ligand binding site. The Mth structure is analyzed in relation to predicted Mth homologs and potential ligand binding features.
Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan.,West AP Jr, Llamas LL, Snow PM, Benzer S, Bjorkman PJ Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3744-9. Epub 2001 Mar 13. PMID:11274391[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ West AP Jr, Llamas LL, Snow PM, Benzer S, Bjorkman PJ. Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3744-9. Epub 2001 Mar 13. PMID:11274391 doi:10.1073/pnas.051625298
